1MFV
Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-03-31 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.91 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.681, 73.197, 134.448 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.16854 |
| Rwork | 0.167 |
| R-free | 0.19489 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb code 1smd |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.317 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.091 | 0.370 |
| Number of reflections | 34179 | |
| <I/σ(I)> | 32 | 5.8 |
| Completeness [%] | 96.7 | 98.9 |
| Redundancy | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | vapordiffusion, combined with soaking with inhibitor at 1 mM concentration | 9 | 298 | 40% MPD, pH 9.0, vapordiffusion, combined with soaking with inhibitor at 1 mM concentration, temperature 298K |
